Probing the Function of Viral Fusion Proteins with Synthetic Peptides

Abstract

Synthetic peptides offer several unique approaches to studying molecular and cellular interactions. Not only do these peptides provide A. large quantity of material for experimental analysis, but they also offer A. degree of homogeneity that is difficult to obtain through routine biochemical purification. Only during the last several years has the ability to use these peptides for dissecting biochemical interactions begun to be explored. For example, synthetic peptides are now being utilized frequently to generate antisera specific for sequenced genes. This approach has been successfully applied to detecting and characterizing viral and cellular proteins (Neumann et al., 1985; Walter et al., 1981; Walter and Doolittle, 1983) as well as to generate neutralizing antibodies in animals (Chow et al., 1985). In addition to serving as an antigenic stimulus, however, peptides may be used as A. biochemical probe to analyze molecular interactions, either as agonists or antagonists. The functional domain of epidermal growth factor involved in cell stimulation has been delineated by the methodical use of small peptides to mimic the effect of the intact molecule (Komoriya et al, 1984). Complex interactions such as cell binding to the substratum have been brought to A. more elementary level by realizing that the peptide Asp XX Gly serves as an apparent fibronectin attachment site (Pierschbacher and Ruoslahti, 1984).

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